Apoptosis, a programmed, cell-autonomous death process, plays important roles in a variety of physiological and pathological events.1
These range from normal fetal development to diseases, such as cancer2
organ failure and neurodegenerative diseases. During apoptosis, caspases execute the disassembly of cellular components by proteolytic cleavage of a variety of substrates, such as poly-(ADP ribose) polymerase,3
DNA-dependent protein kinase (DNA-PK), topoisomerases, and protein kinase C delta.4
At least ten caspases have been discovered. Some of these caspases identify and cleave a specific peptide substrate, while others recognize the same peptide substrate.4
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- Thornberry, NA. and Y. Lazebnik, Science 281, 1312-1316 (1998).
- Reed, JC. J. Clin. Oncol. 17, 2941-2953 (1999).
- Lazebnik, YA. et al. Nature 371, 346-347 (1994).
- Villa, P. et al. Trends Biochem. Sci. 22, 388-393 (1997).